Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly.

@article{Canzio2011ChromodomainmediatedOO,
  title={Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly.},
  author={Daniele Canzio and Evelyn Y Chang and Smita Shankar and Kristopher M. Kuchenbecker and Matthew D Simon and Hiten D Madhani and Geeta J Narlikar and Bassem Al-Sady},
  journal={Molecular cell},
  year={2011},
  volume={41 1},
  pages={67-81}
}
HP1 proteins are central to the assembly and spread of heterochromatin containing histone H3K9 methylation. The chromodomain (CD) of HP1 proteins specifically recognizes the methyl mark on H3 peptides, but the same extent of specificity is not observed within chromatin. The chromoshadow domain of HP1 proteins promotes homodimerization, but this alone cannot explain heterochromatin spread. Using the S. pombe HP1 protein, Swi6, we show that recognition of H3K9-methylated chromatin in vitro relies… CONTINUE READING

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Heterochromatin revisited

Nature Reviews Genetics • 2007
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